- Purification and Characterization of the α-Glucosidase Produced by Thermophilic Fungus Thermoascus aurantiacus CBMAI 756
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Ana Flávia Azevedo Carvalho , Maurício Boscolo , Roberto da Silva , Henrique Ferreira , Eleni Gomes
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J. Microbiol. 2010;48(4):452-459. Published online August 20, 2010
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DOI: https://doi.org/10.1007/s12275-010-9319-2
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Αn α-glucosidase enzyme produced by the fungus Thermoascus aurantiacus CBMAI 756 was purified by ultra filtration, ammonium sulphate precipitation, and chromatography using Q Sepharose, Sephacryl S-200, and Superose 12 columns. The apparent molecular mass of the enzyme was 83 kDa as determined in gel electrophoresis. Maximum activity was observed at pH 4.5 at 70°C. Enzyme showed stability stable in the pH range of 3.0-9.0 and lost 40% of its initial activity at the temperatures of 40, 50, and 60°C. In the presence of ions Na+, Ba2+, Co2+, Ni2+, Mg2+, Mn2+, Al3+, Zn2+, Ca2+ this enzyme maintained 90-105% of its maximum activity and was inhibited by Cr3+, Ag+, and Hg2+. The enzyme showed a transglycosylation property, by the release of oligosaccharides after 3 h of incubation with maltose, and specificity for short maltooligosaccharides and α-PNPG. The Km measured for the α-glucosidase was 0.07 μM, with a Vmax of 318.0 μmol/min/mg.
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Citations
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- A Specific Short Dextrin-Hydrolyzing Extracellular Glucosidase from the Thermophilic Fungus Thermoascus aurantiacus 179-5
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Ana Flavia Azevedo Carvalho , Aline Zorzetto Gonclves , Roberto da Silva , Eleni Gomes
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J. Microbiol. 2006;44(3):276-283.
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DOI: https://doi.org/2385 [pii]
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Abstract
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The thermophilic fungus Thermoascus aurantiacus 179-5 produced large quantities of a glucosidase which preferentially hydrolyzed maltose over starch. Enzyme production was high in submerged fermentation, with a maximal activity of 30 U/ml after 336 h of fermentation. In solid-state fermentation, the activity of the enzyme was 22 U/ml at 144 h in medium containing wheat bran and 5.8 U/ml at 48 h when cassava pulp was used as the culture medium. The enzyme was specific for maltose, very slowly hydrolyzed starch, dextrins (2-7G) and the synthetic substrate (α-PNPG), and did not hydrolyze sucrose. These properties suggest that the enzyme is a type II α-glucosidase. The optimum temperature of the enzyme was 70?. In addition, the enzyme was highly thermostable (100% stability for 10 h at 60? and a half-life of 15 min at 80?), and stable within a wide pH range.
- Production of Saccharogenic and Dextrinogenic Amylases by Rhizomucor pusillus A 13.36
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Tony M. Silva , Derlene Attili-Angelis , Ana Flavia Azevedo Carvalho , Roberto Da Silva , Mauricio Boscolo , Eleni Gomes
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J. Microbiol. 2005;43(6):561-568.
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DOI: https://doi.org/2289 [pii]
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Abstract
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A newly-isolated thermophilic strain of the zygomycete fungus Rhizomucor pusillus 13.36 produced highly active dextrinogenic and saccharogenic enzymes. Cassava pulp was a good alternative substrate for amylase production. Dextrinogenic and saccharogenic amylases exhibited optimum activities at a pH of 4.0-4.5 and 5.0 respectively and at a temperature of 75oC. The enzymes were highly thermostable, with no detectable loss of saccharogenic or dextrinogenic activity after 1 h and 6 h at 60oC, respectively. The saccharogenic activity was inhibited by Ca2+ while the dextrinogenic was indifferent to this ion. Both activities were inhibited by Fe2+ and Cu2+ Hydrolysis of soluble starch by the crude enzyme yielded 66% glucose, 19.5% maltose, 7.7% maltotriose and 6.6% oligosaccharides.
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